ID A9WS59_RENSM Unreviewed; 1013 AA.
AC A9WS59;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:ABY24188.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:ABY24188.1};
GN OrderedLocusNames=RSal33209_2462 {ECO:0000313|EMBL:ABY24188.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY24188.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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DR EMBL; CP000910; ABY24188.1; -; Genomic_DNA.
DR AlphaFoldDB; A9WS59; -.
DR STRING; 288705.RSal33209_2462; -.
DR KEGG; rsa:RSal33209_2462; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_11; -.
DR OMA; EFMVQYA; -.
DR Proteomes; UP000002007; Chromosome.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR InterPro; IPR023057; GlnE.
DR InterPro; IPR005190; GlnE_rpt_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE/ADENYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 2.
DR Pfam; PF03710; GlnE; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:ABY24188.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ABY24188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW Transferase {ECO:0000313|EMBL:ABY24188.1}.
FT DOMAIN 88..337
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 361..505
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 610..846
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 871..1010
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 1013 AA; 110505 MW; 278D7EB4248D898E CRC64;
MGQATMVKSL PRVLIEQGFA DLEKSTRFLA VPELLDFAQD DLFAGLAFAA DPDLALQSLV
RMLAAPAELA ERVARLVQAG PKRSEPMFRL LGASEALADF LIRNPGQSAA LEISVSAEPV
GVPGKVLRTS LLQAVGADPE SATPLSGLGT AEATTAMRRQ YRRHLTELAI RDLCAADPAD
VLPIVAAELA DLAGAALDAA LAIARAELVG TFSAQQVTAV ELAVIGMGKC GARELNYISD
VDVIYVVAAN GLADYDELPI QVGTQLAALL ARIINAPDRE PGLWELDANL RPEGKDGPLV
RTLDSHLEYY RRWASSWEFQ ALLKARPIAG NLALGEQYTS ALAPMIWNSS ERDGFVESVQ
AMRRRVSANI PAEEQNRQLK LGPGGLRDVE FTVQLLQLVH GKADSSLRKQ DTTGAIEALS
TAGYVGRTDA AEFDGAYRYL RVLEHRIQLV HLRRTHLMPV AEPALRALAR SSQGAMAMSR
PSAKVLLDQW QSVKRRVRSL HERIFYRPLL NAAANLSAED ASLSPESAQA RLAALGYQDT
AGAMRHIEAL TTGVSRRAAL QRQLLPVLLD WLGDGVDPDS GLLAFRRLSE SLGTTHWYLG
MLRDSQAAAE RLCHVLSSSH LIADLLEVSP EETKWLGSDK DLRPLSFQAQ WQEIQSKMSR
HPDPSSAMRL IRLIRRREVL RIALADSAGL LDQDAIGTAL GDVDRAAVLG ALHVAENQQD
EAKTDVLVVA MGRQGGREIG YGSDADVLFV HKARPGVDPA GAQAQAVQIV SQLSALLTQP
LKPAIRAERV LAIDADLRPE GKNGALVRSL DSYREYYGRW SLIWEAQALL RARPMAGSDE
LAAEFMALVD SVRYPDQLSE QDLREVRRVK ARVESERLPR GADPARQIKL GRGGLSDVEW
LVQLLQLQHA RAQVQLRTTS TLTALSGLAE LGFVADEDAD ALAKAWRLAS RIRSANVLWT
GRGSDSLPSS RRDLEAVARW CGYPPGHGGA FEEDYLRITR QARAVFERLF YGE
//